P53618 (COPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coatomer subunit beta

Alternative name(s):
Beta-coat protein
Short name=Beta-COP

Gene names

Name:	COPB1
Synonyms:	COPB
ORF Names:	MSTP026

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	953 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis By similarity. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. Ref.10 Ref.12 Ref.14 Ref.16
Subunit structure	Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-terminus) with HIV-1 Nef; the interaction is direct. Interacts with SCYL1. Interacts with COPG1. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct. Interacts with KCNK2/TREK (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2/TREK. Interacts with anthrax lethal factor (LF); this interaction may facilitate endosomal vesicle membrane translocation of LF and its release from the lumen of endosomal vesicles to external milieu. Interacts with CAPN8 and PRKCE By similarity. Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes By similarity. Interacts with STX17 By similarity. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle › COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane. Endoplasmic reticulum-Golgi intermediate compartment. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm By similarity. Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack By similarity. Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae By similarity. Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles By similarity. Some association with high-density and low-density microsomes and mitochondria/nuclei fraction By similarity. Very little found in plasma membrane fraction By similarity. Ref.7 Ref.8 Ref.9 Ref.10 Ref.15 Ref.16
Post-translational modification	Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8 By similarity.
Miscellaneous	Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.
Sequence similarities	Contains 6 HEAT repeats.

Ontologies

Keywords
Biological process	ER-Golgi transport Host-virus interaction Protein transport Transport
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane
Domain	Repeat
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	COPI coating of Golgi vesicle Traceable author statement. Source: Reactome intra-Golgi vesicle-mediated transport Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein transport Inferred from electronic annotation. Source: InterPro retrograde vesicle-mediated transport, Golgi to ER Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	COPI vesicle coat Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 953	953	Coatomer subunit beta		PRO_0000193833
Regions
	Repeat	96 – 131	36	HEAT 1
	Repeat	132 – 168	37	HEAT 2
	Repeat	240 – 276	37	HEAT 3
	Repeat	277 – 314	38	HEAT 4
	Repeat	316 – 353	38	HEAT 5
	Repeat	396 – 433	38	HEAT 6
Experimental info
	Sequence conflict	825	1	D → E in AAD41240. Ref.1
	Sequence conflict	825	1	D → E in CAA57622. Ref.6
	Sequence conflict	847	1	F → L in AAD41240. Ref.1
	Sequence conflict	847	1	F → L in CAA57622. Ref.6
	Sequence conflict	911	1	I → S in AAD41240. Ref.1
	Sequence conflict	911	1	I → S in CAA57622. Ref.6
	Sequence conflict	915	1	I → L in AAD41240. Ref.1
	Sequence conflict	915	1	I → L in CAA57622. Ref.6
	Sequence conflict	925	1	G → V in AAD41240. Ref.1
	Sequence conflict	925	1	G → V in CAA57622. Ref.6
	Sequence conflict	950	1	K → E in AAD41240. Ref.1
	Sequence conflict	950	1	K → E in CAA57622. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P53618 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: BE916C1C5A599D79	FASTA	953	107,142
	10 20 30 40 50 60 MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM 70 80 90 100 110 120 TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST 130 140 150 160 170 180 LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF 190 200 210 220 230 240 LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS 250 260 270 280 290 300 ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI 310 320 330 340 350 360 VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL 370 380 390 400 410 420 KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DNNEAAAADV 430 440 450 460 470 480 LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEIR 490 500 510 520 530 540 RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP 550 560 570 580 590 600 PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 610 620 630 640 650 660 PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE KLSQKKESEK 670 680 690 700 710 720 RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT 730 740 750 760 770 780 GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH 790 800 810 820 830 840 DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF 850 860 870 880 890 900 RQMWAEFEWE NKVTVNTNMV DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 910 920 930 940 950 FGEDALANVS IEKPIHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human beta-cop homolog gene, complete CDS." Zhang J., Liu T., Fu G., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., Jiang Y.X., Zhao X.W., Liu S. , Liu L.S., Ding J.F., Gao R.L., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Aorta.
[3]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[6]	"Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic." Benichou S., Bomsel M., Bodeus M., Durand H., Doute M., Letourneur F., Camonis J., Benarous R. J. Biol. Chem. 269:30073-30076(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 651-953, INTERACTION WITH HIV-1 NEF. Tissue: Lymphoid tissue.
[7]	"The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex." Olivos-Glander I.M., Janne P.A., Nussbaum R.L. Am. J. Hum. Genet. 57:817-823(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Identification and characterization of novel isoforms of COP I subunits." Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K. J. Biochem. 128:793-801(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COPG1, SUBUNIT, SUBCELLULAR LOCATION.
[9]	"Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP." Sun Z., Anderl F., Frohlich K., Zhao L., Hanke S., Brugger B., Wieland F., Bethune J. Traffic 8:582-593(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARF1, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[10]	"Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1." Styers M.L., O'Connor A.K., Grabski R., Cormet-Boyaka E., Sztul E. Am. J. Physiol. 294:C1485-C1498(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic." Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y., Presley J.F., McPherson P.S. J. Biol. Chem. 283:22774-22786(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SCYL1.
[12]	"HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta-COP-dependent pathway in T cells." Schaefer M.R., Wonderlich E.R., Roeth J.F., Leonard J.A., Collins K.L. PLoS Pathog. 4:E1000131-E1000131(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIV-1 NEF.
[13]	"COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro." Tamayo A.G., Bharti A., Trujillo C., Harrison R., Murphy J.R. Proc. Natl. Acad. Sci. U.S.A. 105:5254-5259(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ANTHRAX LETHAL FACTOR.
[14]	"Early endosomes and endosomal coatomer are required for autophagy." Razi M., Chan E.Y., Tooze S.A. J. Cell Biol. 185:305-321(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Enhancement of TREK1 channel surface expression by protein-protein interaction with beta-COP." Kim E., Hwang E.M., Yarishkin O., Yoo J.C., Kim D., Park N., Cho M., Lee Y.S., Sun C.H., Yi G.S., Yoo J., Kang D., Han J., Hong S.G., Park J.Y. Biochem. Biophys. Res. Commun. 395:244-250(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNK2, SUBCELLULAR LOCATION.
[16]	"Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly and reassembly." Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y. J. Biol. Chem. 285:7197-7207(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF084457 mRNA. Translation: AAD41240.1. AF111807 mRNA. Translation: AAL39009.1. AL136593 mRNA. Translation: CAB66528.1. CH471064 Genomic DNA. Translation: EAW68481.1. CH471064 Genomic DNA. Translation: EAW68482.1. CH471064 Genomic DNA. Translation: EAW68483.1. CH471064 Genomic DNA. Translation: EAW68484.1. CH471064 Genomic DNA. Translation: EAW68485.1. BC037280 mRNA. Translation: AAH37280.1. X82103 mRNA. Translation: CAA57622.1.
IPI	IPI00295851.
PIR	A55136. T46913.
RefSeq	NP_001137533.1. NM_001144061.1. NP_001137534.1. NM_001144062.1. NP_057535.1. NM_016451.4.
UniGene	Hs.339278.
3D structure databases
ProteinModelPortal	P53618.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-265N.
IntAct	P53618. 25 interactions.
MINT	MINT-1151935.
STRING	9606.ENSP00000249923.
PTM databases
PhosphoSite	P53618.
Polymorphism databases
DMDM	116241311.
Proteomic databases
PaxDb	P53618.
PeptideAtlas	P53618.
PRIDE	P53618.
Protocols and materials databases
DNASU	1315.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000249923; ENSP00000249923; ENSG00000129083. ENST00000439561; ENSP00000397873; ENSG00000129083.
GeneID	1315.
KEGG	hsa:1315.
UCSC	uc001mlg.2. human.
Organism-specific databases
CTD	1315.
GeneCards	GC11M014436.
H-InvDB	HIX0009466.
HGNC	HGNC:2231. COPB1.
HPA	CAB012338.
MIM	600959. gene.
neXtProt	NX_P53618.
PharmGKB	PA26747.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5096.
HOGENOM	HOG000207417.
HOVERGEN	HBG005380.
InParanoid	P53618.
OMA	DFEWENK.
OrthoDB	EOG4KPT94.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	P53618.
Bgee	P53618.
CleanEx	HS_COPB1.
Genevestigator	P53618.
GermOnline	ENSG00000129083. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR002553. Clathrin/coatomer_adapt-like_N. IPR011710. Coatomer_bsu_C. IPR016460. COPB1. [Graphical view]
PANTHER	PTHR10635. PTHR10635. 1 hit.
Pfam	PF01602. Adaptin_N. 1 hit. PF07718. Coatamer_beta_C. 1 hit. [Graphical view]
PIRSF	PIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	COPB1. human.
GenomeRNAi	1315.
NextBio	5379.
SOURCE	Search...

Entry information

Entry name

COPB_HUMAN

Accession

Primary (citable) accession number: P53618
Secondary accession number(s): D3DQX0 , Q6GTT7, Q9NTK2, Q9UNW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.